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Updated: Nov 22, 2025

Prostaglandin Extraction and Analysis in Caenorhabditis elegans
Published on: June 25, 2013
Investigation of the Substrate-Binding Site of a Prostaglandin E Synthase in Bombyx mori
Kohji Yamamoto1, Aiko Hirowatari2
1Department of Bioscience and Biotechnology, Kyushu University Graduate School, 744 Motooka, Nishi-ku, Fukuoka, 819- 0395, Fukuoka, Japan. yamamok@agr.kyushu-u.ac.jp.
Abstract:
Prostaglandin E synthase (PGES) catalyzes the conversion of prostaglandin H2 to prostaglandin E2 in the presence of glutathione (GSH) in mammals. Amid the limited knowledge on prostaglandin and its related enzymes in insects, we recently identified PGES from the silkworm Bombyx mori (bmPGES) and determined its crystal structure complexed with GSH. In the current study, we investigated the substrate-binding site of bmPGES by site-directed mutagenesis and X-ray crystallography. We found that the residues Tyr107, Val155, Met159, and Glu203 are located in the catalytic pockets of bmPGES, and mutagenesis of each residue reduced the bmPGES activity. Our results suggest that these four residues contribute to the catalytic activity of bmPGES. Overall, this structure-function study holds implications in controlling pests by designing rational and efficient pesticides.
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